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Shrimp (Pandalopsis dispar) waste hydrolysate as a source of novel β–secretase inhibitors Li-Chan, Eunice C Y; Cheung, Imelda W Y; Byun, Hee-Guk
Abstract
In this study, purified peptides from shrimp waste hydrolysates (SWHs) were examined for their inhibitory effects against β–secretase. During consecutive purification using a Sephadex G–25 column chromatography and high performance liquid chromatography on a C18 column, a potent β–secretase inhibitory peptide Asp–Val–Leu–Phe–His (629 Da) was isolated and identified from SWH24 by Q–TOF MS/MS and the IC50 value was determined to be 92.70 μM. The β–secretase inhibition patterns of the purified peptides were found to be competitive. Among synthesized β–secretase inhibitory peptides, Leu–Phe–His had higher β–secretase inhibitory activity than the others. The result of this study suggests that the β–secretase inhibitory peptide derived from SWH24 could be potential candidates to develop nutraceuticals and pharmaceuticals.
Item Metadata
Title |
Shrimp (Pandalopsis dispar) waste hydrolysate as a source of novel β–secretase inhibitors
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Creator | |
Publisher |
BioMed Central
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Date Issued |
2016-04-25
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Description |
In this study, purified peptides from shrimp waste hydrolysates (SWHs) were examined for their inhibitory effects against β–secretase. During consecutive purification using a Sephadex G–25 column chromatography and high performance liquid chromatography on a C18 column, a potent β–secretase inhibitory peptide Asp–Val–Leu–Phe–His (629 Da) was isolated and identified from SWH24 by Q–TOF MS/MS and the IC50 value was determined to be 92.70 μM. The β–secretase inhibition patterns of the purified peptides were found to be competitive. Among synthesized β–secretase inhibitory peptides, Leu–Phe–His had higher β–secretase inhibitory activity than the others. The result of this study suggests that the β–secretase inhibitory peptide derived from SWH24 could be potential candidates to develop nutraceuticals and pharmaceuticals.
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Subject | |
Genre | |
Type | |
Language |
eng
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Date Available |
2018-06-11
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Provider |
Vancouver : University of British Columbia Library
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Rights |
Attribution 4.0 International (CC BY 4.0)
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DOI |
10.14288/1.0368608
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URI | |
Affiliation | |
Citation |
Fisheries and Aquatic Sciences. 2016 Apr 25;19(1):11
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Publisher DOI |
10.1186/s41240-016-0008-x
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Peer Review Status |
Reviewed
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Scholarly Level |
Faculty
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Copyright Holder |
Li-Chan et al.
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Rights URI | |
Aggregated Source Repository |
DSpace
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Item Media
Item Citations and Data
Rights
Attribution 4.0 International (CC BY 4.0)